Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
2004-5-31
pubmed:abstractText
Resorption of amino acids in kidney and intestine is mediated by transporters, which prefer groups of amino acids with similar physico-chemical properties. It is generally assumed that most neutral amino acids are transported across the apical membrane of epithelial cells by system B(0). Here we have characterized a novel member of the Na(+)-dependent neurotransmitter transporter family (B(0)AT1) isolated from mouse kidney, which shows all properties of system B(0). Flux experiments showed that the transporter is Na(+)-dependent, electrogenic, and actively transports most neutral amino acids but not anionic or cationic amino acids. Superfusion of mB(0)AT1-expressing oocytes with neutral amino acids generated inward currents, which were proportional to the fluxes observed with labeled amino acids. In situ hybridization showed strong expression in intestinal microvilli and in the proximal tubule of the kidney. Expression of mouse B(0)AT1 was restricted to kidney, intestine, and skin. It is generally assumed that mutations of the system B(0) transporter underlie autosomal recessive Hartnup disorder. In support of this notion mB(0)AT1 is located on mouse chromosome 13 in a region syntenic to human chromosome 5p15, the locus of Hartnup disorder. Thus, the human homologue of this transporter is an excellent functional and positional candidate for Hartnup disorder.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
24467-76
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:15044460-Amino Acid Sequence, pubmed-meshheading:15044460-Amino Acid Transport Systems, pubmed-meshheading:15044460-Amino Acid Transport Systems, Neutral, pubmed-meshheading:15044460-Amino Acids, pubmed-meshheading:15044460-Animals, pubmed-meshheading:15044460-Anions, pubmed-meshheading:15044460-Base Sequence, pubmed-meshheading:15044460-Biological Transport, pubmed-meshheading:15044460-Cations, pubmed-meshheading:15044460-Cloning, Molecular, pubmed-meshheading:15044460-DNA, Complementary, pubmed-meshheading:15044460-Electrophysiology, pubmed-meshheading:15044460-Hartnup Disease, pubmed-meshheading:15044460-Hydrogen-Ion Concentration, pubmed-meshheading:15044460-In Situ Hybridization, pubmed-meshheading:15044460-Intestines, pubmed-meshheading:15044460-Ions, pubmed-meshheading:15044460-Kidney, pubmed-meshheading:15044460-Leucine, pubmed-meshheading:15044460-Mice, pubmed-meshheading:15044460-Mice, Inbred C57BL, pubmed-meshheading:15044460-Mice, Inbred DBA, pubmed-meshheading:15044460-Models, Biological, pubmed-meshheading:15044460-Models, Genetic, pubmed-meshheading:15044460-Molecular Sequence Data, pubmed-meshheading:15044460-Mutation, pubmed-meshheading:15044460-Oocytes, pubmed-meshheading:15044460-Peptides, pubmed-meshheading:15044460-Phylogeny, pubmed-meshheading:15044460-Plasmids, pubmed-meshheading:15044460-Protein Structure, Tertiary, pubmed-meshheading:15044460-RNA, Complementary, pubmed-meshheading:15044460-RNA, Messenger, pubmed-meshheading:15044460-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:15044460-Skin, pubmed-meshheading:15044460-Substrate Specificity, pubmed-meshheading:15044460-Time Factors
pubmed:year
2004
pubmed:articleTitle
Molecular cloning of mouse amino acid transport system B0, a neutral amino acid transporter related to Hartnup disorder.
pubmed:affiliation
School of Biochemistry and Molecular Biology, Australian National University, Canberra ACT 0200, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't